ID A0A3T4RMW8_SALET Unreviewed; 491 AA. AC A0A3T4RMW8; DT 08-MAY-2019, integrated into UniProtKB/TrEMBL. DT 08-MAY-2019, sequence version 1. DT 29-SEP-2021, entry version 11. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000256|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000256|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000256|HAMAP-Rule:MF_00920, GN ECO:0000313|EMBL:EBP4056412.1}; GN ORFNames=Z599_01310 {ECO:0000313|EMBL:EBP4056412.1}; OS Salmonella enterica I. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=59201 {ECO:0000313|EMBL:EBP4056412.1}; RN [1] {ECO:0000313|EMBL:EBP4056412.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=MDH-2013-00175 {ECO:0000313|EMBL:EBP4056412.1}; RG GenomeTrakr network: Whole genome sequencing for foodborne pathogen traceback; RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Acts as a receptor for the CC complex formed by the signal recognition particle (SRP) and the CC ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the CC transfer of the RNC complex to the Sec translocase for insertion into CC the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the CC dissociation of the SRP-FtsY complex into the individual components. CC {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SUBUNIT: Part of the signal recognition particle protein translocation CC system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein CC composed of Ffh and a 4.5S RNA molecule. {ECO:0000256|HAMAP- CC Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00920}; CC Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00920}. Cytoplasm CC {ECO:0000256|HAMAP-Rule:MF_00920}. Membrane CC {ECO:0000256|ARBA:ARBA00004287}; Peripheral membrane protein CC {ECO:0000256|ARBA:ARBA00004287}; Cytoplasmic side CC {ECO:0000256|ARBA:ARBA00004287}. CC -!- DOMAIN: Contains an acidic N-terminal A domain, a central N domain and CC a C-terminal GTPase G domain that can bind and hydrolyze GTP. Contains CC at least two lipid-binding sites. The first site contains the first 14 CC amino acids (helix 1) and the second binding site is an amphipathic CC alpha-helix located at the interface between the A- and the N-domain CC (helix 2). {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00920}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:EBP4056412.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AAGLQK010000001; EBP4056412.1; -; Genomic_DNA. DR RefSeq; WP_001528170.1; NZ_QAPU01000004.1. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-UniRule. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 1.20.120.140; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00920; FtsY; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004390; SR_rcpt_FtsY. DR InterPro; IPR036225; SRP/SRP_N. DR InterPro; IPR000897; SRP54_GTPase_dom. DR InterPro; IPR042101; SRP54_N_sf. DR PANTHER; PTHR43134:SF7; PTHR43134:SF7; 1. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47364; SSF47364; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00064; ftsY; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|HAMAP-Rule:MF_00920}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00920}; KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP- KW Rule:MF_00920}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00920}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00920}; KW Receptor {ECO:0000256|ARBA:ARBA00023170, ECO:0000256|HAMAP-Rule:MF_00920}. FT DOMAIN 461..474 FT /note="SRP54" FT /evidence="ECO:0000259|PROSITE:PS00300" FT NP_BIND 294..301 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT NP_BIND 376..380 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT NP_BIND 440..443 FT /note="GTP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00920" FT REGION 1..58 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 70..89 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 384..404 FT /evidence="ECO:0000256|SAM:Coils" FT COMPBIAS 19..33 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 491 AA; 53777 MW; 1D43F7DB77B2D8E3 CRC64; MAKQKKRGFF SWLGFGDKEQ KQEQTEEQQI VEEQRPVEPP VETAADIDAQ TPAHSKAETE AFAEEVVDVT EKVQESEKPQ PVEPEPATAV ETAAPQIAVE REELLLPEEV KDEAISPEEW QAEAETVEVI AAVEEEGENA AKFTDEELEA QALAAQAAEE AVMVVPPAEE DAPVEAIVQE QEKPTKEGFF ARLKRSLLKT KENLGSGFIS LFRGKKIDDD LFEELEEQLL IADVGVETTR KIIANLTEGA SRKQLKDAEA LYGLLKDEMG EILAKVDEPL NIEGKTPFVI LMVGVNGVGK TTTIGKLARQ FEQQGKSVML AAGDTFRAAA VEQLQVWGQR NNIPVIAQHT GADSASVIFD AIQAAKARNV DVLIADTAGR LQNKSHLMEE LKKIVRVMKK LDEEAPHEVM LTIDASTGQN AVSQAKLFHE AVGLTGITLT KLDGTAKGGV IFSVADQFGI PIRYIGVGER IEDLRPFKAD DFIEALFARE D //